Q96FL9 (GLT14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 14
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 14
Short name=GalNAc-T14
Short name=pp-GaNTase 14
Protein-UDP acetylgalactosaminyltransferase 14
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14

Gene names

Name:	GALNT14
ORF Names:	UNQ2434/PRO4994

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Highly expressed in fetal and adult kidney. Widely expressed at low level. Weakly expressed in whole brain, cerebellum, thymus, lung, mammary gland, liver, stomach, small intestine, colon, pancreas, spleen, bladder, uterus, placenta, testis, ovary, skeletal muscle, leukocyte, B-cell, bone marrow, fetal brain, fetal thymus, fetal lung, fetal liver, fetal small intestine, fetal spleen, fetal skeletal and fetus. Ref.1
Domain	There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.
Sequence caution	The sequence BAB14795.1 differs from that shown. Reason: Chimeric at the C-terminus.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96FL9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Major isoform.

Isoform 2 (identifier: Q96FL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-132: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q96FL9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     44-99: PSDADWDDLW...NRAIPDTRHL → VWSLFFKVAG...HLQTQVFLQV

Note: Minor isoform.

Isoform 4 (identifier: Q96FL9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPK → MSFPMSLARSSVPFADSGLSSSQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Polypeptide N-acetylgalactosaminyltransferase 14		PRO_0000059133
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 26	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 552	526	Lumenal Potential
	Domain	415 – 550	136	Ricin B-type lectin
	Region	110 – 215	106	Catalytic subdomain A
	Region	274 – 336	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	430 ↔ 449		By similarity
	Disulfide bond	476 ↔ 493		By similarity
	Disulfide bond	517 ↔ 538		By similarity
Natural variations
	Alternative sequence	1 – 43	43	MRRLT…VQTPK → MSFPMSLARSSVPFADSGLS SSQ in isoform 4.		VSP_045121
	Alternative sequence	44 – 99	56	PSDAD…DTRHL → VWSLFFKVAGMSPWAPQVPV SPTPPYQRGHLPTGGHLAVC HFPCLLQEAQFHLQTQVFLQ V in isoform 3.		VSP_011221
	Alternative sequence	100 – 132	33	Missing in isoform 2.		VSP_011222
	Natural variant	469	1	Q → K. Corresponds to variant rs2288101 [ dbSNP | Ensembl ].		VAR_033948
Experimental info
	Sequence conflict	368	1	Q → R in BAB14795. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 6F2ABAA89F482696	FASTA	552	64,321
	10 20 30 40 50 60 MRRLTRRLVL PVFGVLWITV LLFFWVTKRK LEVPTGPEVQ TPKPSDADWD DLWDQFDERR 70 80 90 100 110 120 YLNAKKWRVG DDPYKLYAFN QRESERISSN RAIPDTRHLR CTLLVYCTDL PPTSIIITFH 130 140 150 160 170 180 NEARSTLLRT IRSVLNRTPT HLIREIILVD DFSNDPDDCK QLIKLPKVKC LRNNERQGLV 190 200 210 220 230 240 RSRIRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFTYIE 250 260 270 280 290 300 SASELRGGFD WSLHFQWEQL SPEQKARRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDM 310 320 330 340 350 360 DMDIWGGENF EISFRVWMCG GSLEIVPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE 370 380 390 400 410 420 VWMDEYKQYY YAARPFALER PFGNVESRLD LRKNLRCQSF KWYLENIYPE LSIPKESSIQ 430 440 450 460 470 480 KGNIRQRQKC LESQRQNNQE TPNLKLSPCA KVKGEDAKSQ VWAFTYTQQI LQEELCLSVI 490 500 510 520 530 540 TLFPGAPVVL VLCKNGDDRQ QWTKTGSHIE HIASHLCLDT DMFGDGTENG KEIVVNPCES 550 SLMSQHWDMV SS
	Isoform 2 [UniParc]. Checksum: 9028631165BC7C08	FASTA	519	60,520
	10 20 30 40 50 60 MRRLTRRLVL PVFGVLWITV LLFFWVTKRK LEVPTGPEVQ TPKPSDADWD DLWDQFDERR 70 80 90 100 110 120 YLNAKKWRVG DDPYKLYAFN QRESERISSN RAIPDTRHLS VLNRTPTHLI REIILVDDFS 130 140 150 160 170 180 NDPDDCKQLI KLPKVKCLRN NERQGLVRSR IRGADIAQGT TLTFLDSHCE VNRDWLQPLL 190 200 210 220 230 240 HRVKEDYTRV VCPVIDIINL DTFTYIESAS ELRGGFDWSL HFQWEQLSPE QKARRLDPTE 250 260 270 280 290 300 PIRTPIIAGG LFVIDKAWFD YLGKYDMDMD IWGGENFEIS FRVWMCGGSL EIVPCSRVGH 310 320 330 340 350 360 VFRKKHPYVF PDGNANTYIK NTKRTAEVWM DEYKQYYYAA RPFALERPFG NVESRLDLRK 370 380 390 400 410 420 NLRCQSFKWY LENIYPELSI PKESSIQKGN IRQRQKCLES QRQNNQETPN LKLSPCAKVK 430 440 450 460 470 480 GEDAKSQVWA FTYTQQILQE ELCLSVITLF PGAPVVLVLC KNGDDRQQWT KTGSHIEHIA 490 500 510 SHLCLDTDMF GDGTENGKEI VVNPCESSLM SQHWDMVSS
	Isoform 3 [UniParc]. Checksum: 6968DC02A2AAF2F4	FASTA	557	64,289
	10 20 30 40 50 60 MRRLTRRLVL PVFGVLWITV LLFFWVTKRK LEVPTGPEVQ TPKVWSLFFK VAGMSPWAPQ 70 80 90 100 110 120 VPVSPTPPYQ RGHLPTGGHL AVCHFPCLLQ EAQFHLQTQV FLQVRCTLLV YCTDLPPTSI 130 140 150 160 170 180 IITFHNEARS TLLRTIRSVL NRTPTHLIRE IILVDDFSND PDDCKQLIKL PKVKCLRNNE 190 200 210 220 230 240 RQGLVRSRIR GADIAQGTTL TFLDSHCEVN RDWLQPLLHR VKEDYTRVVC PVIDIINLDT 250 260 270 280 290 300 FTYIESASEL RGGFDWSLHF QWEQLSPEQK ARRLDPTEPI RTPIIAGGLF VIDKAWFDYL 310 320 330 340 350 360 GKYDMDMDIW GGENFEISFR VWMCGGSLEI VPCSRVGHVF RKKHPYVFPD GNANTYIKNT 370 380 390 400 410 420 KRTAEVWMDE YKQYYYAARP FALERPFGNV ESRLDLRKNL RCQSFKWYLE NIYPELSIPK 430 440 450 460 470 480 ESSIQKGNIR QRQKCLESQR QNNQETPNLK LSPCAKVKGE DAKSQVWAFT YTQQILQEEL 490 500 510 520 530 540 CLSVITLFPG APVVLVLCKN GDDRQQWTKT GSHIEHIASH LCLDTDMFGD GTENGKEIVV 550 NPCESSLMSQ HWDMVSS
	Isoform 4 [UniParc]. Checksum: 685DB05D5597341F	FASTA	532	61,588
	10 20 30 40 50 60 MSFPMSLARS SVPFADSGLS SSQPSDADWD DLWDQFDERR YLNAKKWRVG DDPYKLYAFN 70 80 90 100 110 120 QRESERISSN RAIPDTRHLR CTLLVYCTDL PPTSIIITFH NEARSTLLRT IRSVLNRTPT 130 140 150 160 170 180 HLIREIILVD DFSNDPDDCK QLIKLPKVKC LRNNERQGLV RSRIRGADIA QGTTLTFLDS 190 200 210 220 230 240 HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFTYIE SASELRGGFD WSLHFQWEQL 250 260 270 280 290 300 SPEQKARRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDM DMDIWGGENF EISFRVWMCG 310 320 330 340 350 360 GSLEIVPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE VWMDEYKQYY YAARPFALER 370 380 390 400 410 420 PFGNVESRLD LRKNLRCQSF KWYLENIYPE LSIPKESSIQ KGNIRQRQKC LESQRQNNQE 430 440 450 460 470 480 TPNLKLSPCA KVKGEDAKSQ VWAFTYTQQI LQEELCLSVI TLFPGAPVVL VLCKNGDDRQ 490 500 510 520 530 QWTKTGSHIE HIASHLCLDT DMFGDGTENG KEIVVNPCES SLMSQHWDMV SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14." Wang H., Tachibana K., Zhang Y., Iwasaki H., Kameyama A., Chen L., Guo J.-M., Hiruma T., Togayachi A., Kudo T., Kikuchi N., Narimatsu H. Biochem. Biophys. Res. Commun. 300:738-744(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Tissue: Stomach.
[2]	Wandall H.H., Bennett E.P. Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-435 (ISOFORM 2). Tissue: Fibroblast, Retinoblastoma and Teratocarcinoma.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye and Ovary.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 14

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB078144 mRNA. Translation: BAC56889.1. Y09324 mRNA. Translation: CAA70505.4. AY358758 mRNA. Translation: AAQ89118.1. AK022753 mRNA. Translation: BAB14227.1. AK024039 mRNA. Translation: BAB14795.1. Sequence problems. AK091313 mRNA. Translation: BAC03634.1. AK122747 mRNA. Translation: BAG53701.1. AC009301 Genomic DNA. Translation: AAX88899.1. AC009305 Genomic DNA. Translation: AAX93209.1. AC015980 Genomic DNA. Translation: AAY24301.1. CH471053 Genomic DNA. Translation: EAX00489.1. BC006269 mRNA. Translation: AAH06269.2. BC010659 mRNA. Translation: AAH10659.1.
IPI	IPI00041868. IPI00101384. IPI00456717.
RefSeq	NP_001240755.1. NM_001253826.1. NP_001240756.1. NM_001253827.1. NP_078848.2. NM_024572.3.
UniGene	Hs.468058.
3D structure databases
ProteinModelPortal	Q96FL9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000288988.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q96FL9.
Polymorphism databases
DMDM	51316071.
Proteomic databases
PaxDb	Q96FL9.
PRIDE	Q96FL9.
Protocols and materials databases
DNASU	79623.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324589; ENSP00000314500; ENSG00000158089. ENST00000349752; ENSP00000288988; ENSG00000158089. ENST00000356174; ENSP00000348497; ENSG00000158089. ENST00000406653; ENSP00000385435; ENSG00000158089.
GeneID	79623.
KEGG	hsa:79623.
UCSC	uc002rnr.3. human. uc002rns.3. human. uc010ezo.2. human.
Organism-specific databases
CTD	79623.
GeneCards	GC02M031044.
HGNC	HGNC:22946. GALNT14.
HPA	HPA010785.
MIM	608225. gene.
neXtProt	NX_Q96FL9.
PharmGKB	PA134920089.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG239675.
HOVERGEN	HBG051699.
KO	K00710.
OMA	DWDDLWD.
OrthoDB	EOG483D4C.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q96FL9.
Bgee	Q96FL9.
CleanEx	HS_GALNT14.
Genevestigator	Q96FL9.
GermOnline	ENSG00000158089. Homo sapiens.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2_met. IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF02709. Glyco_transf_7C. 1 hit. PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GALNT14. human.
GenomeRNAi	79623.
NextBio	68697.
SOURCE	Search...

Entry information

Entry name

GLT14_HUMAN

Accession

Primary (citable) accession number: Q96FL9
Secondary accession number(s): B3KV89 , Q4ZG75, Q53SU1, Q53TJ0, Q8IVI4, Q9BRH1, Q9H827, Q9H9J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.